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The Journal of Neuroscience, September 15, 1998, 18(18):7178-7188
Dynamic Regulation of RGS2 Suggests a Novel Mechanism in
G-Protein Signaling and Neuronal Plasticity
Tatsuya
Ingi1,
Andrejs
M.
Krumins3,
Peter
Chidiac3,
Greg M.
Brothers4,
Stephen
Chung4,
Bryan E.
Snow4,
Carol A.
Barnes5,
Anthony A.
Lanahan1,
David P.
Siderovski4,
Elliott M.
Ross3,
Alfred G.
Gilman3, and
Paul F.
Worley1, 2
Departments of 1 Neuroscience and
2 Neurology, Johns Hopkins University School of Medicine,
Baltimore, Maryland 21210, 3 Department of Pharmacology,
University of Texas Southwestern Medical Center, Dallas, Texas 75235, 4 Quantitative Biology Laboratory, Amgen Institute,
Toronto, Ontario M5G 2C1, Canada, and 5 Department of
Psychology and Neurology and Division of Neuronal Systems, Memory, and
Aging, University of Arizona, Tucson, Arizona 84724
Long-term neuronal plasticity is known to be dependent on rapid
de novo synthesis of mRNA and protein, and recent
studies provide insight into the molecules involved in this response. Here, we demonstrate that mRNA encoding a member of the regulator of
G-protein signaling (RGS) family, RGS2, is rapidly induced in neurons
of the hippocampus, cortex, and striatum in response to stimuli that
evoke plasticity. Although several members of the RGS family are
expressed in brain with discrete neuronal localizations, RGS2 appears
unique in that its expression is dynamically responsive to neuronal
activity. In biochemical assays, RGS2 stimulates the GTPase activity of
the subunit of Gq and Gi1. The effect on Gi1 was observed only after reconstitution of the protein
in phospholipid vesicles containing M2 muscarinic acetylcholine
receptors. RGS2 also inhibits both Gq- and
Gi-dependent responses in transfected cells. These studies
suggest a novel mechanism linking neuronal activity and signal
transduction.
Key words:
RGS; immediate early genes; seizure; neuronal plasticity; G-protein; GTPase-activating proteins; MAP kinase
Copyright © 1998 Society for Neuroscience 0270-6474/98/18187178-11$05.00/0
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B. E. Snow, A. M. Krumins, G. M. Brothers, S.-F. Lee, M. A. Wall, S. Chung, J. Mangion, S. Arya, A. G. Gilman, and D. P. Siderovski
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T. Wieland, N. Bahtijari, X.-B. Zhou, C. Kleuss, and M. I. Simon
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M. L. Cunningham, G. L. Waldo, S. Hollinger, J. R. Hepler, and T. K. Harden
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S. P. Heximer, H. Lim, J. L. Bernard, and K. J. Blumer
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S. Choi, H.-J. Kim, Y.-S. Ko, S.-W. Jeong, Y. I. Kim, W. F. Simonds, J.-W. Oh, and S.-Y. Nah
Galpha q/11 Coupled to Mammalian Phospholipase C beta 3-like Enzyme Mediates the Ginsenoside Effect on Ca2+-activated Cl- Current in the Xenopus Oocyte
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A. J. Oliveira-dos-Santos, G. Matsumoto, B. E. Snow, D. Bai, F. P. Houston, I. Q. Whishaw, S. Mariathasan, T. Sasaki, A. Wakeham, P. S. Ohashi, et al.
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E. S. Park, C. O. Echetebu, S. Soloff, and M. S. Soloff
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